The structure of an AspRS–tRNA(Asp) complex reveals a tRNA-dependent control mechanism

The 2.6 Å resolution crystal structure of an inactive complex between yeast tRNA(Asp) and Escherichia coli aspartyl-tRNA synthetase reveals the molecular details of a tRNA-induced mechanism that controls the specificity of the reaction. The dimer is asymmetric, with only one of the two bound tRNAs e...

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Bibliografische gegevens

Gepubliceerd in:	EMBO J
Hoofdauteurs:	Moulinier, L., Eiler, S., Eriani, G., Gangloff, J., Thierry, J.-C., Gabriel, K., McClain, W.H., Moras, D.
Formaat:	Artigo
Taal:	Inglês
Gepubliceerd in:	Nature Publishing Group 2001
Onderwerpen:	Article
Online toegang:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC125622/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11566892/ https://ncbi.nlm.nih.govhttps://doi.org/10.1093/emboj/20.18.5290
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